Structure of PDB 3u6w Chain A Binding Site BS01

Receptor Information

>3u6w Chain A (length=399) Species: 83332 (Mycobacterium tuberculosis H37Rv)

IVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRVI
DRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSAS
QTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVHF
YNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSPE
SYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSIE
WMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGER
TGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYGG
DLVYTAFSGSHQDAINKGLDAMKDVDDMLWQVPYLPIDPRDVGRTYEAV

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 3u6w Chain A Residue 426

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3u6w Removal of the C-terminal regulatory domain of alpha-isopropylmalate synthase disrupts functional substrate binding.
• Resolution: 2.21 Å
• Binding residue (original residue number in PDB): D81 H285 H287
• Binding residue (residue number reindexed from 1): D63 H267 H269
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.3.3.13: 2-isopropylmalate synthase.

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0003852 2-isopropylmalate synthase activity
• GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer

Biological Process

• GO:0009098 L-leucine biosynthetic process
• GO:0019752 carboxylic acid metabolic process

External links

• PDB: RCSB:3u6w, PDBe:3u6w, PDBj:3u6w
• PDBsum: 3u6w
• PubMed: 22352945
• UniProt: P9WQB3|LEU1_MYCTU 2-isopropylmalate synthase (Gene Name=leuA)